Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway.
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Apoptosis in pancreatic β-islet cells in Type 2 diabetesNeuroendocrine hormone amylin in diabetesMechanisms of islet amyloidosis toxicity in type 2 diabetesThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPAmylin at the interface between metabolic and neurodegenerative disordersOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesHsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes TreatmentUCHL1 deficiency exacerbates human islet amyloid polypeptide toxicity in β-cells: evidence of interplay between the ubiquitin/proteasome system and autophagyEarly amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Calcium-activated calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes.Drosophila melanogaster as a model system for studies of islet amyloid polypeptide aggregation.Autophagy defends pancreatic β cells from human islet amyloid polypeptide-induced toxicityNeuroinflammation and neurologic deficits in diabetes linked to brain accumulation of amylin.Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.Amylin deposition in the brain: A second amyloid in Alzheimer disease?β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency.The Mitochondrial Peptidase Pitrilysin Degrades Islet Amyloid Polypeptide in Beta-Cells.Cyclin-dependent kinase 5 promotes pancreatic β-cell survival via Fak-Akt signaling pathways.Age related changes in pancreatic beta cells: A putative extra-cerebral site of Alzheimer's pathology.Structural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat modelNovel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease.β-cell loss and β-cell apoptosis in human type 2 diabetes are related to islet amyloid deposition.Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic β-cells: protective role of p62-positive cytoplasmic inclusionsIslet amyloid polypeptide is a target antigen for diabetogenic CD4+ T cells.Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptideType 2 diabetes as a protein misfolding disease.X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-MicroglobulinKisspeptin prevention of amyloid-β peptide neurotoxicity in vitro.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.β-Cell failure in type 2 diabetes: a case of asking too much of too few?Islet β cell mass in diabetes and how it relates to function, birth, and death.CHOP Contributes to, But Is Not the Only Mediator of, IAPP Induced β-Cell ApoptosisAdsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated AggregationDegradation of islet amyloid polypeptide by neprilysin.β-Cell Deficit in Obese Type 2 Diabetes, a Minor Role of β-Cell Dedifferentiation and Degranulation.A common landscape for membrane-active peptides.
P2860
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P2860
Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway.
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Evidence for proteotoxicity in ...... arly in the secretory pathway.
@ast
Evidence for proteotoxicity in ...... arly in the secretory pathway.
@en
type
label
Evidence for proteotoxicity in ...... arly in the secretory pathway.
@ast
Evidence for proteotoxicity in ...... arly in the secretory pathway.
@en
prefLabel
Evidence for proteotoxicity in ...... arly in the secretory pathway.
@ast
Evidence for proteotoxicity in ...... arly in the secretory pathway.
@en
P2093
P2860
P1476
Evidence for proteotoxicity in ...... arly in the secretory pathway.
@en
P2093
Chang-jiang Huang
Charles G Glabe
Howard A Reber
Michael W Yeh
O Joe Hines
Sergey Ryazantsev
Tatyana Gurlo
Timothy D O'Brien
P2860
P304
P356
10.2353/AJPATH.2010.090532
P407
P577
2009-12-30T00:00:00Z